SAP97 increases Kv1.5 currents through an indirect N‐terminal mechanism

@article{Eldstrom2003SAP97IK,
  title={SAP97 increases Kv1.5 currents through an indirect N‐terminal mechanism},
  author={Jodene Eldstrom and Woo S. Choi and David F. Steele and David Fedida},
  journal={FEBS Letters},
  year={2003},
  volume={547}
}
A specific N-terminal residue in Kv1.5 is required for upregulation of the channel by SAP97.
Kif5b is an essential forward trafficking motor for the Kv1.5 cardiac potassium channel
TLDR
Kif5b is essential to anterograde trafficking of a cardiac voltage‐gated potassium channel, and the dominant negative acts by indirectly inhibiting endocytosis.
Kv1.5 channels are regulated by PKC-mediated endocytic degradation
The anchoring protein SAP97 retains Kv1.5 channels in the plasma membrane of cardiac myocytes.
TLDR
SAP97 regulates the K(+) current in cardiac myocytes by retaining and immobilizing Kv1.5 subunits in the plasma membrane, and this new regulatory mechanism may contribute to the targeting of Kv channels in cardiacMyocytes.
The C-Terminal PDZ-Binding Motif in the Kv1.5 Potassium Channel Governs its Modulation by the Na+/H+ Exchanger Regulatory Factor 2
TLDR
The results suggest that NHERFs might participate in the regulation of electrical excitability in part by controlling Kv1.5 surface abundance and by clustering signal transduction molecules to the channel.
Modulation of human Kv1.5 channel kinetics by N-cadherin.
Activation of voltage gated K⁺ channel Kv1.5 by β-catenin.
The role of the T1 domain in the trafficking of Kv1.5
The T1 domain of Kv channels is important in the subfamily-specific assembly by clustering individual monomers to increase their chances of interaction into tetramers. Furthermore, T1 domain plays
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SAP97 interacts with Kv1.5 in heterologous expression systems.
TLDR
The results suggest that SAP97 may play an important role in the modulation of Kv1.5 channel function in cardiac myocytes and the interactions of these polypeptides with a cardiac voltage-gated potassium channel.
Inward rectifier potassium channel Kir2.2 is associated with synapse-associated protein SAP97.
TLDR
A direct association is identified of Kir2.2.3 with the MAGUK family member SAP97 that may form part of a macromolecular signaling complex in many different tissues.
Surface Expression of Kv1 Channels Is Governed by a C-terminal Motif*
TLDR
The newly identified C-terminal motif governs processing and cell surface expression of Kv1 voltage-gated K+ channels and the action of the essential sequence is shown to be independent of the chaperone effect of KVβ subunits.
Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases
TLDR
Functional and biochemical evidence is presented that cell-surface clustering of Shaker-subfamily K+ channels is mediated by the PSD-95 family of membrane-associated putative guanylate kinases, and the ability of PDZ domains to function as independent modules for protein–protein interaction, and their presence in other junction-associated molecules suggest that PDZ-domain-containing polypeptides may be widely involved in the organization of proteins at sites of membrane specialization.
Phosphorylation of Serine‐880 in GluR2 by Protein Kinase C Prevents Its C Terminus from Binding with Glutamate Receptor‐Interacting Protein
TLDR
It is shown that the C terminus of GluR2 of the α‐amino‐3‐hydroxy‐5‐methylisoxazole‐4‐propionate (AMPA) receptor is phosphorylated by protein kinase C and that serine‐880 is the major phosphorylation site.
Psd-95 and Sap97 Exhibit Distinct Mechanisms for Regulating K+ Channel Surface Expression and Clustering
TLDR
Data show that ion channel clustering by PSD-95 and SAP97 occurs by distinct mechanisms, and suggests that these channel-clustering proteins may play diverse roles in regulating the abundance and distribution of channels at synapses and other neuronal membrane specializations.
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